phosphofructokinase
Sign in to savePhosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
Research
8,342 papers- Phosphofructokinase.Advances in enzymology and related areas of molecular biology · 1979
- Phosphofructokinase.Current topics in cellular regulation · 1972
- Structural basis for allosteric regulation of human phosphofructokinase-1.Nature communications · 2024
- Isozymes of phosphofructokinase.Isozymes · 1982
- [Phosphofructokinase (PFK)].Nihon rinsho. Japanese journal of clinical medicine · 1995
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Encyclopedic overview
7 sectionsContents
- Function
- Phosphofructokinase family
- Clinical significance
- Regulation
- See also
- References
- External links
Phosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
== Function == The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. Phosphofructokinase catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. It is allosterically inhibited by ATP and allosterically activated by AMP, thus indicating the cell's energetic needs when it undergoes the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha- (PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation.
Excerpted from Wikipedia’s “phosphofructokinase” article, available under the CC BY-SA 4.0 licence.